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UniProtKB - P21672 (RIR3_YEAST)

Protein

Ribonucleoside-diphosphate reductase large chain 2

Gene

RNR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.1 Publication

Miscellaneous

Two distinct regulatory sites have been defined: the specificity site, which controls substrate specificity, and the activity site which regulates overall catalytic activity. A substrate-binding catalytic site, located on R1, is formed only in the presence of the second subunit R2 (By similarity).By similarity
Present with 1364 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Under complex allosteric control mediated by deoxynucleoside triphosphates and ATP binding to separate specificity and activation sites on the large subunit. The type of nucleotide bound at the specificity site determines substrate preference. It seems probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP reduction and dTTP favors GDP reduction. Stimulated by ATP and inhibited by dATP binding to the activity site (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: DNA replication

This protein is involved in the pathway DNA replication, which is part of Genetic information processing.
View all proteins of this organism that are known to be involved in the pathway DNA replication and in Genetic information processing.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei5Allosteric activatorBy similarity1
Binding sitei53Allosteric activatorBy similarity1
Binding sitei88Allosteric activatorBy similarity1
Binding sitei202SubstrateBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei218Important for hydrogen atom transferBy similarity1
Sitei226Allosteric effector binding, determines substrate specificityBy similarity1
Binding sitei247Substrate; via amide nitrogenBy similarity1
Sitei256Allosteric effector binding, determines substrate specificityBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei426Proton acceptorBy similarity1
Active sitei428Cysteine radical intermediateBy similarity1
Active sitei430Proton acceptorBy similarity1
Sitei443Important for hydrogen atom transferBy similarity1
Sitei741Important for electron transferBy similarity1
Sitei742Important for electron transferBy similarity1
Sitei864Interacts with thioredoxin/glutaredoxinBy similarity1
Sitei867Interacts with thioredoxin/glutaredoxinBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor Source: GO_Central
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • deoxyribonucleotide biosynthetic process Source: SGD
  • DNA replication Source: UniProtKB-UniPathway
View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Oxidoreductase
Biological processDNA replication
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:YIL066C-MONOMER
YEAST:YIL066C-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-499943 Interconversion of nucleotide di- and triphosphates

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00326

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ribonucleoside-diphosphate reductase large chain 2 (EC:1.17.4.1)
Alternative name(s):
Ribonucleotide reductase DNA damage-inducible regulatory subunit 2
Ribonucleotide reductase R1 subunit 2
Ribonucleotide reductase large subunit 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RNR3
Synonyms:DIN1
Ordered Locus Names:YIL066C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome IX

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001328 RNR3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001872041 – 869Ribonucleoside-diphosphate reductase large chain 2Add BLAST869

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi218 ↔ 443Redox-activeBy similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei227PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei806PhosphoserineCombined sources1
Modified residuei827PhosphoserineBy similarity1
Modified residuei868PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P21672

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P21672

PRoteomics IDEntifications database

More...PRIDEi		P21672

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P21672

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Highly induced by DNA-damage.2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterotetramer of two large (R1) and two small (R2) subunits. S.cerevisiae has two different R1 subunits (RNR1 and RNR3) and two different R2 subunits (RNR2 and RNR4). The functional form of the small subunits is a RNR2-RNR4 heterodimer, where RNR2 provides the iron-radical center and RNR4 is required for proper folding of RNR2 and assembly with the large subunits. Under normal growth conditions, the active form of the large subunits is a homodimer of the constitutively expressed RNR1. In damaged cells or cells arrested for DNA synthesis, the reductase consists of multiple species because of the association of the small subunits (RNR2-RNR4) with either the RNR1 homodimer or a heterodimer of RNR1 and the damage-inducible RNR3.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		34926, 87 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1103 Ribonucleoside-diphosphate reductase variant 2

Database of interacting proteins

More...DIPi		DIP-2563N

Protein interaction database and analysis system

More...IntActi		P21672, 32 interactors

Molecular INTeraction database

More...MINTi		P21672

STRING: functional protein association networks

More...STRINGi		4932.YIL066C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P21672

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P21672

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 92ATP-conePROSITE-ProRule annotationAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni11 – 17Allosteric activator bindingBy similarity7
Regioni217 – 218Substrate bindingBy similarity2
Regioni285 – 288Allosteric effector binding, determines substrate specificityBy similarity4
Regioni426 – 430Substrate bindingBy similarity5
Regioni607 – 611Substrate bindingBy similarity5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ribonucleoside diphosphate reductase large chain family.Curated

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00910000144246

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000057035

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P21672

KEGG Orthology (KO)

More...KOi		K10807

Identification of Orthologs from Complete Genome Data

More...OMAi		LEIWHID

Database of Orthologous Groups

More...OrthoDBi		EOG092C0QYB

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1

The PANTHER Classification System

More...PANTHERi		PTHR11573 PTHR11573, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 1 hit
PF00317 Ribonuc_red_lgN, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01183 RIBORDTASEM1

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48168 SSF48168, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02506 NrdE_NrdA, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P21672-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MYVIKRDGRK EPVQFDKITS RITRLSYGLD PNRIDAVKVT QRIISGVYSG 
        60         70         80         90        100
VTTVELDNLA AETCAYMTTV HPDYATLAAR IAISNLHKQT TKQFSKVIED 
       110        120        130        140        150
LHDWINPATG KHAPMISDEI YNIVMENKDT LNSAIVYDRD FQYTYFGFKT 
       160        170        180        190        200
LERSYLLRLN GEVAERPQHL VMRVALGIHG SDIESVLKTY NLMSLRYFTH 
       210        220        230        240        250
ASPTLFNAGT PHPQMSSCFL IAMKDDSIEG IYDTLKECAM ISKTAGGVGL 
       260        270        280        290        300
HINNIRSTGS YIAGTNGTSN GLIPMIRVFN NTARYVDQGG NKRPGAFALF 
       310        320        330        340        350
LEPWHADIFD FVDIRKTHGK EEIRARDLFP ALWIPDLFMK RVQEDGPWTL 
       360        370        380        390        400
FSPSAAPGLD DVWGDEFEEL YTRYEREGRG KTIKAQKLWY AILQAQTETG 
       410        420        430        440        450
TPFMVYKDAC NRKTNQQNLG TIKSSNLCCE IVEYSSPDET AVCNLASIAL 
       460        470        480        490        500
PAFVEVSEDG KTASYNFERL HEIAKVITHN LNRVIDRNYY PVPEARNSNM 
       510        520        530        540        550
KHRPIALGVQ GLADTYMMLR LPFESEEAQT LNKQIFETIY HATLEASCEL 
       560        570        580        590        600
AQKEGKYSTF EGSPASKGIL QFDMWNAKPF GMWDWETLRK DIVKHGLRNS 
       610        620        630        640        650
LTMAPMPTAS TSQILGYNEC FEPVTSNMYS RRVLSGEFQV VNPYLLRDLV 
       660        670        680        690        700
DLGIWDDSMK QYLITQNGSI QGLPNVPQEL KELYKTVWEI SQKTIINMAA 
       710        720        730        740        750
DRAIYIDQSH SLNLFLQAPS MGKITSMHFY GWKKGLKTGM YYLRTQAASA 
       760        770        780        790        800
AIQFTIDQEV ADQAATHIAS VSELDRPVYV PKGTKFSEQK AASALTESSD 
       810        820        830        840        850
NEKDASPVPS EQSSVSSAMS NVKLEDSVAP AVPTETIKED SDEKKCDIYN 
       860 
EKVIACTAPT PEACESCSG
Length:869
Mass (Da):97,515
Last modified:February 1, 1995 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBEE8DEDE41D7049A
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA34569 differs from that shown. Reason: Frameshift at positions 127, 129, 130, 247, 250, 287 and 313.Curated
The sequence CAA86157 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti21 – 22RI → VL no nucleotide entry (PubMed:2199320).Curated2
Sequence conflicti37V → F no nucleotide entry (PubMed:2199320).Curated1
Sequence conflicti58N → I no nucleotide entry (PubMed:2199320).Curated1
Sequence conflicti69T → H no nucleotide entry (PubMed:2199320).Curated1
Sequence conflicti83I → T no nucleotide entry (PubMed:2199320).Curated1
Sequence conflicti212H → L in AAA34569 (PubMed:2204819).Curated1
Sequence conflicti249G → V in AAA34569 (PubMed:2204819).Curated1
Sequence conflicti311F → K in AAA34569 (PubMed:2204819).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Z38060 Genomic DNA Translation: CAA86157.1 Different initiation.
M58012 Genomic DNA Translation: AAA34569.1 Frameshift.
BK006942 Genomic DNA Translation: DAA08484.1

Protein sequence database of the Protein Information Resource

More...PIRi		S48413 WMBY3L

NCBI Reference Sequences

More...RefSeqi		NP_012198.3, NM_001179416.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YIL066C_mRNA; YIL066C_mRNA; YIL066C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854744

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YIL066C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38060 Genomic DNA Translation: CAA86157.1 Different initiation.
M58012 Genomic DNA Translation: AAA34569.1 Frameshift.
BK006942 Genomic DNA Translation: DAA08484.1
PIRiS48413 WMBY3L
RefSeqiNP_012198.3, NM_001179416.3

3D structure databases

ProteinModelPortaliP21672
SMRiP21672
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34926, 87 interactors
ComplexPortaliCPX-1103 Ribonucleoside-diphosphate reductase variant 2
DIPiDIP-2563N
IntActiP21672, 32 interactors
MINTiP21672
STRINGi4932.YIL066C

PTM databases

iPTMnetiP21672

Proteomic databases

MaxQBiP21672
PaxDbiP21672
PRIDEiP21672

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL066C_mRNA; YIL066C_mRNA; YIL066C
GeneIDi854744
KEGGisce:YIL066C

Organism-specific databases

SGDiS000001328 RNR3

Phylogenomic databases

GeneTreeiENSGT00910000144246
HOGENOMiHOG000057035
InParanoidiP21672
KOiK10807
OMAiLEIWHID
OrthoDBiEOG092C0QYB

Enzyme and pathway databases

UniPathwayi
UPA00326

BioCyciMetaCyc:YIL066C-MONOMER
YEAST:YIL066C-MONOMER
ReactomeiR-SCE-499943 Interconversion of nucleotide di- and triphosphates

Miscellaneous databases

Protein Ontology

More...PROi		PR:P21672

Family and domain databases

InterProiView protein in InterPro
IPR005144 ATP-cone_dom
IPR013346 NrdE_NrdA
IPR000788 RNR_lg_C
IPR013509 RNR_lsu_N
IPR008926 RNR_R1-su_N
IPR039718 Rrm1
PANTHERiPTHR11573 PTHR11573, 1 hit
PfamiView protein in Pfam
PF03477 ATP-cone, 1 hit
PF02867 Ribonuc_red_lgC, 1 hit
PF00317 Ribonuc_red_lgN, 1 hit
PRINTSiPR01183 RIBORDTASEM1
SUPFAMiSSF48168 SSF48168, 1 hit
TIGRFAMsiTIGR02506 NrdE_NrdA, 1 hit
PROSITEiView protein in PROSITE
PS51161 ATP_CONE, 1 hit
PS00089 RIBORED_LARGE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRIR3_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21672
Secondary accession number(s): D6VVL8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1995
Last modified: December 5, 2018
This is version 182 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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